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P39929 (SNF7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vacuolar-sorting protein SNF7
Alternative name(s):
DOA4-independent degradation protein 1
Vacuolar protein-sorting-associated protein 32
Gene names
Name:SNF7
Synonyms:DID1, VPS32
Ordered Locus Names:YLR025W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Appears to sequester MVB cargo. Recruits BRO1, which in turn recruits DOA4, which deubiquitinates cargos before their enclosure within MVB vesicles. Ref.5 Ref.6

Subunit structure

Self-associates. Core component of the ESCRT-III complex (endosomal sorting required for transport complex III). ESCRT-III appears to be sequentially assembled as a flat lattice on the endosome membrane and forms a transient 450 kDa complex that contains DID4, oligomerized SNF7, VPS20 and VPS24. SNF7 oligomerization into a membrane-associated filament is nucleated by association of SNF7 with VPS20; the process is terminated through association of VPS24, possibly by capping the SNF7 filament. VPS24 subsequently associates with DID4/VPS2. Interacts with VTA1; the interaction requires DID2. Interacts with BRO1. Ref.6 Ref.8 Ref.9 Ref.10

Subcellular location

Cytoplasm. Endosome membrane; Peripheral membrane protein Ref.6.

Miscellaneous

Present with 3270 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the SNF7 family.

Caution

Was originally (Ref.1) thought to be a nuclear protein and mutations were shown to prevent full derepression of the SUC2 (invertase) gene.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240Vacuolar-sorting protein SNF7
PRO_0000211446

Regions

Compositional bias68 – 714Poly-Lys
Compositional bias216 – 22813Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue721Phosphothreonine Ref.11 Ref.12
Modified residue1191Phosphoserine Ref.14
Modified residue1931Phosphoserine Ref.14

Experimental info

Sequence conflict1731E → G in AAS56528. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P39929 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 5241A18BB181F0C1

FASTA24026,987
        10         20         30         40         50         60 
MWSSLFGWTS SNAKNKESPT KAIVRLREHI NLLSKKQSHL RTQITNQENE ARIFLTKGNK 

        70         80         90        100        110        120 
VMAKNALKKK KTIEQLLSKV EGTMESMEQQ LFSIESANLN LETMRAMQEG AKAMKTIHSG 

       130        140        150        160        170        180 
LDIDKVDETM DEIREQVELG DEISDAISRP LITGANEVDE DELDEELDML AQENANQETS 

       190        200        210        220        230        240 
KIVNNNVNAA PISENKVSLP SVPSNKIKQS ENSVKDGEEE EDEEDEDEKA LRELQAEMGL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular and genetic analysis of the SNF7 gene in Saccharomyces cerevisiae."
Tu J., Vallier L.G., Carlson M.
Genetics 135:17-23(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins."
Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.
J. Cell Sci. 114:2395-2404(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting."
Babst M., Katzmann D.J., Estepa-Sabal E.J., Meerloo T., Emr S.D.
Dev. Cell 3:271-282(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE ESCRT-III COMPLEX, INTERACTION WITH VPS20, SUBCELLULAR LOCATION.
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae."
Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P., Stevens T.H.
Traffic 5:194-210(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRO1.
[9]"Structural basis for endosomal targeting by the Bro1 domain."
Kim J., Sitaraman S., Hierro A., Beach B.M., Odorizzi G., Hurley J.H.
Dev. Cell 8:937-947(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRO1.
[10]"Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body."
Lottridge J.M., Flannery A.R., Vincelli J.L., Stevens T.H.
Proc. Natl. Acad. Sci. U.S.A. 103:6202-6207(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VTA1.
[11]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[12]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation."
Teis D., Saksena S., Emr S.D.
Dev. Cell 15:578-589(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSEMBLY OF THE ESCRT-III COMPLEX.
[14]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L09751 Genomic DNA. No translation available.
Z73197 Genomic DNA. Translation: CAA97548.1.
AY558202 Genomic DNA. Translation: AAS56528.1.
BK006945 Genomic DNA. Translation: DAA09343.1.
PIRS52590.
RefSeqNP_013125.1. NM_001181912.1.

3D structure databases

ProteinModelPortalP39929.
SMRP39929. Positions 20-95, 121-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31299. 105 interactions.
DIPDIP-1747N.
IntActP39929. 25 interactions.
MINTMINT-389266.
STRING4932.YLR025W.

Proteomic databases

MaxQBP39929.
PaxDbP39929.
PeptideAtlasP39929.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR025W; YLR025W; YLR025W.
GeneID850712.
KEGGsce:YLR025W.

Organism-specific databases

CYGDYLR025w.
SGDS000004015. SNF7.

Phylogenomic databases

eggNOGNOG291419.
GeneTreeENSGT00390000005006.
HOGENOMHOG000209960.
KOK12194.
OMAENEARIF.
OrthoDBEOG72RN9W.

Enzyme and pathway databases

BioCycYEAST:G3O-32186-MONOMER.

Gene expression databases

GenevestigatorP39929.

Family and domain databases

InterProIPR005024. Snf7.
[Graphical view]
PfamPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio966772.
PROP39929.

Entry information

Entry nameSNF7_YEAST
AccessionPrimary (citable) accession number: P39929
Secondary accession number(s): D6VY27, E9P8V6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families